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| Type |
Oral Presentation |
| Area |
Oral Presentation of Young Analytical Chemists Ⅰ |
| Room No. |
303호 |
| Time |
THU 10:02-: |
| Code |
ANAL1.O-24 |
| Subject |
The structural characterization of disease related human transmembrane proteins using the NMR spectroscopy |
| Authors |
조성진, 김지선, 김용애*
한국외국어대학교 화학과, Korea
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| Abstract |
Transmembrane proteins play critical roles in biological processes such as ion transport, channel formation, signaling and cell to cell interaction. In human cells, they are commonly targets for pharmaceuticals. Despite their importance, structural and functional studies of transmembrane proteins have been a difficult task due to the membranous properties and limited amount of material available. So, it remains a lack of biophysical and structural data.
We tried to obtain large quantities of transmembrane domain from human amyloid beta protein (hAβ-TM) and second transmembrane domain from human melanocortin-4 receptor (hMC4R-TM2). The hAβ-TM shows membrane-bound oligomeric state, and the Ca2+-permeable ion channel formation of non-fibrillar state in the cell membrane. So these channels can disrupt the normal cellular calcium homeostasis. It causes pathogenesis of dementia and Alzheimer disease. The hMC4R is located primarily in the brain and regulatory role in food intake and energy homeostasis. Heterozygous mutation D90N located in second transmembrane domain of hMC4R results in human obesity, hyperphagia and insulin resistance.
In this research, we succeed to produce hAβ-TM and hMC4R-TM2. Structural characterizations of these proteins in the membrane environments were obtained by 1D/2D solution and solid-state NMR spectroscopy. We also present the optimized design, construction, and efficiency of a home-built 800 MHz narrow-bore (NB) 1H-15N solid-state NMR probe. 1H-15N 2D SAMPI4 spectra from membrane proteins in oriented bicelles was successfully obtained by using these solid-state NMR probe.
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| E-mail |
sungjin9111@naver.com |
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119th General Meeting of the KCS